ID C6SAC7_NEIME Unreviewed; 217 AA.
AC C6SAC7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=SCO1/SenC family protein {ECO:0000313|EMBL:CBA03777.1};
GN ORFNames=NME_0238 {ECO:0000313|EMBL:CBA03777.1};
OS Neisseria meningitidis alpha153.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=663926 {ECO:0000313|EMBL:CBA03777.1};
RN [1] {ECO:0000313|EMBL:CBA03777.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha153 {ECO:0000313|EMBL:CBA03777.1};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; AM889137; CBA03777.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SAC7; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR PANTHER; PTHR12151:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..217
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005668726"
FT DOMAIN 54..217
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 33..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 92..96
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 217 AA; 23241 MW; 1DC153A50A01A093 CRC64;
MFSVPRSFLP GVFVLAALAA CKPQDNSAAQ VASSSASASA AENAAKPQTR GTDMRKEDIG
GDFTLTDGEG KPFSLSDLKG KVVILSFGFT HCPDVCPTEL LTYSDTLKQL GGQAKDVKVV
FVSIDPERDT PEIIGKYAKQ FNPDFIGLTA TGDQNLPVIK QQYRVVSAKV NQKDDSENYL
VDHSSGAYLI DKNGEVAIFS PYGSEPETIA ADVRTLL
//